A study of the proposed mechanism enantioselective esterification of chiral alcohols by lipase enzymes in organic solvents. Initially the esterification of synthetically useful chiral auxiliaries of the 8- phenylementhol type by commercially available Candida rugosa will be studied. Racemic trans-2-substituted cyclohexanols will be synthesized by expoxide ring opening of cyclohexene oxides. These alcohols will be resolved and the rate of esterification of each enantiomer with lipase will be measured. Kinetic constants will be correlated to computer-generated electrostatic parameters to construct a three dimensional model of the enzyme's active site with respect to theses alcohol substrates. Along with X-ray structures of the lipase, the model will be used to understand the mechanism of enantioselective esterification of alcohols by Candida rugosa lipase. The alcohols resolved in this work will be evaluated as chiral auxiliaries and incorporated into stationary phases to separate enantiomer by chiral- column HPLC. These activities are important to the synthesis of biologically active compounds.